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Publication DatePLoS ONE, ISSN 1932-6203, 03/2016, Volume 11, Issue 3, p. e0150893
Serum amyloid A (SAA) is an evolutionary highly conserved acute phase protein that is predominantly secreted by hepatocytes. However, its role in liver injury...
APOPTOSIS | HUMAN NEUTROPHILS | ACUTE-PHASE REACTANT | RAT-LIVER FIBROSIS | MULTIDISCIPLINARY SCIENCES | SECRETION | MONOCYTE CHEMOTACTIC PROTEIN-1 | A SAA PROTEIN | NF-KAPPA-B | EXPRESSION | INTESTINAL EPITHELIAL-CELLS | Cholestasis - genetics | Cholestasis - metabolism | Serum Amyloid A Protein - pharmacology | Carbon Tetrachloride | Humans | Hepatic Stellate Cells - metabolism | Male | NF-kappa B - metabolism | Liver Cirrhosis - chemically induced | Proto-Oncogene Proteins c-akt - genetics | Matrix Metalloproteinase 9 - metabolism | Ligation | MAP Kinase Kinase 4 - metabolism | I-kappa B Kinase - metabolism | Matrix Metalloproteinase 9 - genetics | Mitogen-Activated Protein Kinase 1 - genetics | Liver Cirrhosis - metabolism | Chemokine CCL2 - metabolism | Chemokine CCL5 - metabolism | Cell Death - drug effects | Proto-Oncogene Proteins c-akt - metabolism | Liver Cirrhosis - genetics | Hepatic Stellate Cells - pathology | Disease Models, Animal | Hepatic Stellate Cells - drug effects | Mitogen-Activated Protein Kinase 3 - genetics | Signal Transduction | Gene Expression Regulation | Rats | Chemokine CCL2 - genetics | Inflammation | I-kappa B Kinase - genetics | Rats, Sprague-Dawley | Cholestasis - pathology | Animals | Mitogen-Activated Protein Kinase 3 - metabolism | NF-kappa B - genetics | Chemokine CCL5 - genetics | Liver Cirrhosis - pathology | MAP Kinase Kinase 4 - genetics | Cell Proliferation - drug effects | Mice, Inbred BALB C | Primary Cell Culture | Mitogen-Activated Protein Kinase 1 - metabolism | Biochemistry | RNA | Cell death | Luciferase | Cell proliferation | Animal models | Transcription factors | Transcription | RANTES | Liver | Carbon tetrachloride | Cytotoxicity | AKT protein | Kinases | Caspase-3 | Proteins | Signal transduction | Immunology | Rodents | Hepatology | Gastroenterology | Fibroblasts | Amyloid | NF-κB protein | Stellate cells | Cytokines | Mortality | Neutrophils | Extracellular signal-regulated kinase | c-Jun protein | Caspase | Poly(ADP-ribose) polymerase | CCL4 protein | Bile duct | Gelatinase B | Medicine | Antibiotics | Hepatocytes | Surgeons | Skin | Annexin V | Monocyte chemoattractant protein 1 | Apoptosis
APOPTOSIS | HUMAN NEUTROPHILS | ACUTE-PHASE REACTANT | RAT-LIVER FIBROSIS | MULTIDISCIPLINARY SCIENCES | SECRETION | MONOCYTE CHEMOTACTIC PROTEIN-1 | A SAA PROTEIN | NF-KAPPA-B | EXPRESSION | INTESTINAL EPITHELIAL-CELLS | Cholestasis - genetics | Cholestasis - metabolism | Serum Amyloid A Protein - pharmacology | Carbon Tetrachloride | Humans | Hepatic Stellate Cells - metabolism | Male | NF-kappa B - metabolism | Liver Cirrhosis - chemically induced | Proto-Oncogene Proteins c-akt - genetics | Matrix Metalloproteinase 9 - metabolism | Ligation | MAP Kinase Kinase 4 - metabolism | I-kappa B Kinase - metabolism | Matrix Metalloproteinase 9 - genetics | Mitogen-Activated Protein Kinase 1 - genetics | Liver Cirrhosis - metabolism | Chemokine CCL2 - metabolism | Chemokine CCL5 - metabolism | Cell Death - drug effects | Proto-Oncogene Proteins c-akt - metabolism | Liver Cirrhosis - genetics | Hepatic Stellate Cells - pathology | Disease Models, Animal | Hepatic Stellate Cells - drug effects | Mitogen-Activated Protein Kinase 3 - genetics | Signal Transduction | Gene Expression Regulation | Rats | Chemokine CCL2 - genetics | Inflammation | I-kappa B Kinase - genetics | Rats, Sprague-Dawley | Cholestasis - pathology | Animals | Mitogen-Activated Protein Kinase 3 - metabolism | NF-kappa B - genetics | Chemokine CCL5 - genetics | Liver Cirrhosis - pathology | MAP Kinase Kinase 4 - genetics | Cell Proliferation - drug effects | Mice, Inbred BALB C | Primary Cell Culture | Mitogen-Activated Protein Kinase 1 - metabolism | Biochemistry | RNA | Cell death | Luciferase | Cell proliferation | Animal models | Transcription factors | Transcription | RANTES | Liver | Carbon tetrachloride | Cytotoxicity | AKT protein | Kinases | Caspase-3 | Proteins | Signal transduction | Immunology | Rodents | Hepatology | Gastroenterology | Fibroblasts | Amyloid | NF-κB protein | Stellate cells | Cytokines | Mortality | Neutrophils | Extracellular signal-regulated kinase | c-Jun protein | Caspase | Poly(ADP-ribose) polymerase | CCL4 protein | Bile duct | Gelatinase B | Medicine | Antibiotics | Hepatocytes | Surgeons | Skin | Annexin V | Monocyte chemoattractant protein 1 | Apoptosis
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Loading RightsJournal of Hepatology, ISSN 0168-8278, 2011, Volume 56, Issue 1, pp. 184 - 191
Background & Aims Mosaic G-protein alpha-subunit ( GNAS )-activating mutations are responsible for the McCune–Albright (MCA) syndrome. This oncogene that...
Gastroenterology and Hepatology | CRP | interleukine 6 signal transducer | GTP | C-reactive protein | jun N-terminal kinase | serum amyloid A | JNK | macroregenerative nodule | complementary deoxyribonucleic acid | MRN | mitogen activated proteins kinase | cAMP | glycoprotein 130 | neuroendocrine secretory protein 55 | hepatocyte nuclear factor 1A | G-protein alpha stimulatory subunit | cDNA | gp130 | protein kinase A | hepatocellular carcinoma | β catenin | IHCA | McCune-Albright syndrome | HCA | PKA | HCC | MAP kinase | MCA | HNF1A | inflammatory hepatocellular adenoma | SAA | cyclic adenosine monophosphate | hepatocellular adenoma | GNAS | CTNNB1 | NESP55 | guanosine-5′-triphosphate | IL6ST | INACTIVATION | PATHWAY | HEPATOCELLULAR ADENOMA | GS-ALPHA | GROWTH | CLASSIFICATION | HUMAN CANCERS | MCCUNE-ALBRIGHT-SYNDROME | GASTROENTEROLOGY & HEPATOLOGY | G-PROTEIN | BINDING | Liver Neoplasms - classification | Humans | Middle Aged | Adenoma, Liver Cell - pathology | Male | Fibrous Dysplasia, Polyostotic - genetics | GTP-Binding Protein alpha Subunits, Gs - genetics | Chromogranins | DNA Mutational Analysis | Base Sequence | Carcinoma, Hepatocellular - genetics | Adult | Female | Liver Neoplasms - pathology | Adenoma, Liver Cell - genetics | STAT3 Transcription Factor - metabolism | Liver Neoplasms - genetics | Signal Transduction | Adenoma, Liver Cell - metabolism | Models, Biological | Carcinoma, Hepatocellular - pathology | Liver Neoplasms - metabolism | Aged | DNA, Neoplasm - genetics | Mutation | Carcinoma, Hepatocellular - metabolism | Liver cancer | Genetic aspects | Nucleic acids | Adenylic acid | Mitogens | Protein kinases | Index Medicus | GTP-Binding Protein alpha Subunits, Gs | Fibrous Dysplasia, Polyostotic | Liver Neoplasms | Life Sciences | Adenoma, Liver Cell | DNA, Neoplasm | STAT3 Transcription Factor | Carcinoma, Hepatocellular | Cancer
Gastroenterology and Hepatology | CRP | interleukine 6 signal transducer | GTP | C-reactive protein | jun N-terminal kinase | serum amyloid A | JNK | macroregenerative nodule | complementary deoxyribonucleic acid | MRN | mitogen activated proteins kinase | cAMP | glycoprotein 130 | neuroendocrine secretory protein 55 | hepatocyte nuclear factor 1A | G-protein alpha stimulatory subunit | cDNA | gp130 | protein kinase A | hepatocellular carcinoma | β catenin | IHCA | McCune-Albright syndrome | HCA | PKA | HCC | MAP kinase | MCA | HNF1A | inflammatory hepatocellular adenoma | SAA | cyclic adenosine monophosphate | hepatocellular adenoma | GNAS | CTNNB1 | NESP55 | guanosine-5′-triphosphate | IL6ST | INACTIVATION | PATHWAY | HEPATOCELLULAR ADENOMA | GS-ALPHA | GROWTH | CLASSIFICATION | HUMAN CANCERS | MCCUNE-ALBRIGHT-SYNDROME | GASTROENTEROLOGY & HEPATOLOGY | G-PROTEIN | BINDING | Liver Neoplasms - classification | Humans | Middle Aged | Adenoma, Liver Cell - pathology | Male | Fibrous Dysplasia, Polyostotic - genetics | GTP-Binding Protein alpha Subunits, Gs - genetics | Chromogranins | DNA Mutational Analysis | Base Sequence | Carcinoma, Hepatocellular - genetics | Adult | Female | Liver Neoplasms - pathology | Adenoma, Liver Cell - genetics | STAT3 Transcription Factor - metabolism | Liver Neoplasms - genetics | Signal Transduction | Adenoma, Liver Cell - metabolism | Models, Biological | Carcinoma, Hepatocellular - pathology | Liver Neoplasms - metabolism | Aged | DNA, Neoplasm - genetics | Mutation | Carcinoma, Hepatocellular - metabolism | Liver cancer | Genetic aspects | Nucleic acids | Adenylic acid | Mitogens | Protein kinases | Index Medicus | GTP-Binding Protein alpha Subunits, Gs | Fibrous Dysplasia, Polyostotic | Liver Neoplasms | Life Sciences | Adenoma, Liver Cell | DNA, Neoplasm | STAT3 Transcription Factor | Carcinoma, Hepatocellular | Cancer
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Loading RightsPLoS ONE, ISSN 1932-6203, 06/2013, Volume 8, Issue 6, p. e64974
The fibrillation of Serum Amyloid A (SAA) - a major acute phase protein - is believed to play a role in the disease Amyloid A (AA) Amyloidosis. To better...
FIBRIL FORMATION | A-PROTEIN | PHYSIOLOGICAL TEMPERATURE | SAA | ACUTE-PHASE PROTEIN | AMINO-ACID-SEQUENCE | MULTIDISCIPLINARY SCIENCES | DISEASE | SOLUBLE OLIGOMERS | MARGINAL STABILITY | HIGH-DENSITY-LIPOPROTEIN | Serum Amyloid A Protein - chemistry | Protein Structure, Secondary | Protein Isoforms - chemistry | Humans | Protein Multimerization | Methionine | Protein Refolding | Solubility | Models, Molecular | Oligomers | Fluorescence spectroscopy | Atomic force microscopy | Amyloidosis | Amyloidogenesis | Bioengineering | Biotechnology | Atomic beam spectroscopy | Fluorescence | Biochemistry | Agglomeration | Seeding | Proteins | Fibrillation | E coli | Dichroism | Physiology | Colon | Heparan sulfate | Spectroscopy | Oligomerization | Incubation | Inflammation | Interdisciplinary aspects | Apolipoproteins | Circular dichroism | Chemistry | Lipoproteins | Microscopy
FIBRIL FORMATION | A-PROTEIN | PHYSIOLOGICAL TEMPERATURE | SAA | ACUTE-PHASE PROTEIN | AMINO-ACID-SEQUENCE | MULTIDISCIPLINARY SCIENCES | DISEASE | SOLUBLE OLIGOMERS | MARGINAL STABILITY | HIGH-DENSITY-LIPOPROTEIN | Serum Amyloid A Protein - chemistry | Protein Structure, Secondary | Protein Isoforms - chemistry | Humans | Protein Multimerization | Methionine | Protein Refolding | Solubility | Models, Molecular | Oligomers | Fluorescence spectroscopy | Atomic force microscopy | Amyloidosis | Amyloidogenesis | Bioengineering | Biotechnology | Atomic beam spectroscopy | Fluorescence | Biochemistry | Agglomeration | Seeding | Proteins | Fibrillation | E coli | Dichroism | Physiology | Colon | Heparan sulfate | Spectroscopy | Oligomerization | Incubation | Inflammation | Interdisciplinary aspects | Apolipoproteins | Circular dichroism | Chemistry | Lipoproteins | Microscopy
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Loading RightsFEBS Letters, ISSN 0014-5793, 07/2015, Volume 589, Issue 15, pp. 1703 - 1712
Over the last years protein engineering using non-standard amino acids has gained increasing attention. As a result, improved methods are now available,...
Non-standard amino acids | Cell-free protein synthesis | Eukaryotic systems | Cotranslational incorporation | eukaryotic release factor 1 | orthogonal aminoacyl-tRNA synthetase | orthogonal tRNA | OTS | otRNA | sAA | nsAA | eRF1 | CFCF | CECF | orthogonal translation system | Pyl | pyrrolysine | aatRNA | internal ribosome entry site | cell-free protein synthesis | pyrrolysyl-tRNA synthetase | continuous-exchange cell-free | release factor | non-standard amino acid | oRS | continuous-flow cell-free | IRES | aminoacyl-tRNA | CuAAC | CFPS | PylRS | copper-catalyzed alkyne-azide cycloaddition | standard amino acid | BIOCHEMISTRY & MOLECULAR BIOLOGY | POSITION-SPECIFIC INCORPORATION | FREE TRANSLATION | UNNATURAL BASE-PAIR | ORTHOGONAL TRANSFER-RNA | CELL BIOLOGY | SYNTHESIS SYSTEM | IN-VITRO | GENETIC-CODE | BIOPHYSICS | TRANSFER-RNA SYNTHETASE | FREE EXPRESSION | SITE-SPECIFIC INCORPORATION | Cell-Free System | Amino Acids - metabolism | Protein Biosynthesis
Non-standard amino acids | Cell-free protein synthesis | Eukaryotic systems | Cotranslational incorporation | eukaryotic release factor 1 | orthogonal aminoacyl-tRNA synthetase | orthogonal tRNA | OTS | otRNA | sAA | nsAA | eRF1 | CFCF | CECF | orthogonal translation system | Pyl | pyrrolysine | aatRNA | internal ribosome entry site | cell-free protein synthesis | pyrrolysyl-tRNA synthetase | continuous-exchange cell-free | release factor | non-standard amino acid | oRS | continuous-flow cell-free | IRES | aminoacyl-tRNA | CuAAC | CFPS | PylRS | copper-catalyzed alkyne-azide cycloaddition | standard amino acid | BIOCHEMISTRY & MOLECULAR BIOLOGY | POSITION-SPECIFIC INCORPORATION | FREE TRANSLATION | UNNATURAL BASE-PAIR | ORTHOGONAL TRANSFER-RNA | CELL BIOLOGY | SYNTHESIS SYSTEM | IN-VITRO | GENETIC-CODE | BIOPHYSICS | TRANSFER-RNA SYNTHETASE | FREE EXPRESSION | SITE-SPECIFIC INCORPORATION | Cell-Free System | Amino Acids - metabolism | Protein Biosynthesis
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Loading RightsFish and Shellfish Immunology, ISSN 1050-4648, 06/2017, Volume 65, pp. 267 - 277
Three serum amyloid A (SAA) genes were identified from the common carp ( ) by PCR and RT-PCR. Considering both direction and sequence similarity with mammal's...
Serum amyloid A | Cyprinus carpio | Recombinant protein | Gene expression | Cloning | Antibacterial effect | MOLECULAR CHARACTERIZATION | PROTEIN | ZEBRAFISH | RECEPTOR | IMMUNOLOGY | ACUTE-PHASE RESPONSE | SAA | FISHERIES | MARINE & FRESHWATER BIOLOGY | SEQUENCE | GENES | VETERINARY SCIENCES | INFECTION | INNATE IMMUNITY | Amino Acid Sequence | Serum Amyloid A Protein - metabolism | Fish Proteins - chemistry | Serum Amyloid A Protein - pharmacology | Escherichia coli - drug effects | Bacteria - drug effects | DNA, Complementary - genetics | Synteny | Transcriptome | Fish Proteins - metabolism | Serum Amyloid A Protein - genetics | Phylogeny | Sequence Alignment - veterinary | Aeromonas hydrophila - physiology | Fish Proteins - genetics | Animals | Serum Amyloid A Protein - chemistry | Cloning, Molecular | Anti-Bacterial Agents - pharmacology | Carps - genetics | Staphylococcus aureus - drug effects | DNA, Complementary - metabolism | Aeromonas hydrophila - drug effects | Platypus | Liver | Escherichia coli | Antibacterial agents | Proteins | Cladistic analysis | Analysis | Fishes | Bacteria | Skin | Protein binding | Bacterial infections | Genes | Recombinant proteins | Genetic research
Serum amyloid A | Cyprinus carpio | Recombinant protein | Gene expression | Cloning | Antibacterial effect | MOLECULAR CHARACTERIZATION | PROTEIN | ZEBRAFISH | RECEPTOR | IMMUNOLOGY | ACUTE-PHASE RESPONSE | SAA | FISHERIES | MARINE & FRESHWATER BIOLOGY | SEQUENCE | GENES | VETERINARY SCIENCES | INFECTION | INNATE IMMUNITY | Amino Acid Sequence | Serum Amyloid A Protein - metabolism | Fish Proteins - chemistry | Serum Amyloid A Protein - pharmacology | Escherichia coli - drug effects | Bacteria - drug effects | DNA, Complementary - genetics | Synteny | Transcriptome | Fish Proteins - metabolism | Serum Amyloid A Protein - genetics | Phylogeny | Sequence Alignment - veterinary | Aeromonas hydrophila - physiology | Fish Proteins - genetics | Animals | Serum Amyloid A Protein - chemistry | Cloning, Molecular | Anti-Bacterial Agents - pharmacology | Carps - genetics | Staphylococcus aureus - drug effects | DNA, Complementary - metabolism | Aeromonas hydrophila - drug effects | Platypus | Liver | Escherichia coli | Antibacterial agents | Proteins | Cladistic analysis | Analysis | Fishes | Bacteria | Skin | Protein binding | Bacterial infections | Genes | Recombinant proteins | Genetic research
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Loading Rights2012, Progress in Molecular Biology and Translational Science, ISBN 9780123945969, Volume 105, 38
Acute phase proteins (APP) were first identified in the early 1900s as early reactants to infectious disease. They are now understood to be an integral part of...
Serum amyloid A | Acute phase protein | C-reactive protein | Haptoglobin | Acute phase response | C-REACTIVE PROTEIN | FELINE INFECTIOUS PERITONITIS | PASTEURELLA-HAEMOLYTICA INFECTION | ESCHERICHIA-COLI LIPOPOLYSACCHARIDE | SAA TURBIDIMETRIC IMMUNOASSAY | LIPOPOLYSACCHARIDE-BINDING PROTEIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | SERUM-AMYLOID-A | TROUT ONCORHYNCHUS-MYKISS | NF-KAPPA-B | ALPHA-1-ACID GLYCOPROTEIN CONCENTRATION | Acute-Phase Reaction - immunology | Animals | Acute-Phase Proteins - immunology
Serum amyloid A | Acute phase protein | C-reactive protein | Haptoglobin | Acute phase response | C-REACTIVE PROTEIN | FELINE INFECTIOUS PERITONITIS | PASTEURELLA-HAEMOLYTICA INFECTION | ESCHERICHIA-COLI LIPOPOLYSACCHARIDE | SAA TURBIDIMETRIC IMMUNOASSAY | LIPOPOLYSACCHARIDE-BINDING PROTEIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | SERUM-AMYLOID-A | TROUT ONCORHYNCHUS-MYKISS | NF-KAPPA-B | ALPHA-1-ACID GLYCOPROTEIN CONCENTRATION | Acute-Phase Reaction - immunology | Animals | Acute-Phase Proteins - immunology
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Loading RightsDevelopmental and Comparative Immunology, ISSN 0145-305X, 2001, Volume 25, Issue 8, pp. 725 - 743
Tissue trauma or invasion by pathogens or parasites induce changes in the quantities of several macromolecules in animal body fluids. These changes comprise...
CRP | Acute phase protein | SAA | Transferrin | Pre-cerebellin-like protein | Acute phase response | Fibrinogen | Fish | Innate immunity | Inflammation | TCBP1 | acute phase response | C-REACTIVE PROTEIN | RAINBOW-TROUT | fibrinogen | AEROMONAS-SALMONICIDA | transferrin | IMMUNOLOGY | CATFISH ICTALURUS-PUNCTATUS | CARP CYPRINUS-CARPIO | PLEURONECTES-PLATESSA L | SERUM CONCENTRATIONS | ZOOLOGY | pre-cerebellin-like protein | innate immunity | inflammation | fish | AMYLOID-P-COMPONENT | TROUT ONCORHYNCHUS-MYKISS | acute phase protein | ATLANTIC SALMON | Serum Amyloid P-Component - immunology | alpha-Macroglobulins - physiology | Acute-Phase Reaction - immunology | alpha-Macroglobulins - immunology | alpha-Macroglobulins - genetics | Molecular Sequence Data | Serum Amyloid P-Component - physiology | Serum Amyloid A Protein - genetics | Transferrin - physiology | Acute-Phase Proteins - genetics | Transferrin - genetics | Acute-Phase Proteins - physiology | Fishes - immunology | Transferrin - immunology | Apolipoproteins - genetics | Fishes - physiology | Amino Acid Sequence | Fishes - genetics | Environmental Monitoring | Complement C3 - metabolism | C-Reactive Protein - genetics | Muramidase - metabolism | Apolipoproteins - immunology | C-Reactive Protein - physiology | Serum Amyloid A Protein - immunology | Sequence Homology, Amino Acid | Serum Amyloid P-Component - genetics | Animals | Apolipoproteins - physiology | C-Reactive Protein - immunology | Serum Amyloid A Protein - physiology | Acute-Phase Proteins - immunology
CRP | Acute phase protein | SAA | Transferrin | Pre-cerebellin-like protein | Acute phase response | Fibrinogen | Fish | Innate immunity | Inflammation | TCBP1 | acute phase response | C-REACTIVE PROTEIN | RAINBOW-TROUT | fibrinogen | AEROMONAS-SALMONICIDA | transferrin | IMMUNOLOGY | CATFISH ICTALURUS-PUNCTATUS | CARP CYPRINUS-CARPIO | PLEURONECTES-PLATESSA L | SERUM CONCENTRATIONS | ZOOLOGY | pre-cerebellin-like protein | innate immunity | inflammation | fish | AMYLOID-P-COMPONENT | TROUT ONCORHYNCHUS-MYKISS | acute phase protein | ATLANTIC SALMON | Serum Amyloid P-Component - immunology | alpha-Macroglobulins - physiology | Acute-Phase Reaction - immunology | alpha-Macroglobulins - immunology | alpha-Macroglobulins - genetics | Molecular Sequence Data | Serum Amyloid P-Component - physiology | Serum Amyloid A Protein - genetics | Transferrin - physiology | Acute-Phase Proteins - genetics | Transferrin - genetics | Acute-Phase Proteins - physiology | Fishes - immunology | Transferrin - immunology | Apolipoproteins - genetics | Fishes - physiology | Amino Acid Sequence | Fishes - genetics | Environmental Monitoring | Complement C3 - metabolism | C-Reactive Protein - genetics | Muramidase - metabolism | Apolipoproteins - immunology | C-Reactive Protein - physiology | Serum Amyloid A Protein - immunology | Sequence Homology, Amino Acid | Serum Amyloid P-Component - genetics | Animals | Apolipoproteins - physiology | C-Reactive Protein - immunology | Serum Amyloid A Protein - physiology | Acute-Phase Proteins - immunology
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Loading RightsJournal of Molecular Recognition, ISSN 0952-3499, 07/2015, Volume 28, Issue 7, pp. 413 - 426
Serum amyloid A (SAA) is a multifunctional acute‐phase protein whose concentration in serum increases markedly following a number of chronic inflammatory and...
protein–protein interaction | hCC | SAA | NMR | conformation | ELISA | HCC | Protein-protein interaction | Conformation | protein-protein interaction | PROTEIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | AA AMYLOIDOSIS | PATHOGENESIS | PEPTIDES | BIOPHYSICS | CHANNEL | DISEASE | SECONDARY STRUCTURE | BINDING-SITES | STRUCTURE PREDICTION | AGGREGATION | Protein Structure, Tertiary | Serum Amyloid A Protein - metabolism | Peptides - chemistry | Humans | Alanine - chemistry | Cystatin C - chemistry | Proline - chemistry | Chromatography, Affinity | Peptides - metabolism | Protein Isoforms - metabolism | Serum Amyloid A Protein - chemistry | Protein Isoforms - chemistry | Cystatin C - metabolism | Calorimetry, Differential Scanning | Protein Conformation | Circular Dichroism
protein–protein interaction | hCC | SAA | NMR | conformation | ELISA | HCC | Protein-protein interaction | Conformation | protein-protein interaction | PROTEIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | AA AMYLOIDOSIS | PATHOGENESIS | PEPTIDES | BIOPHYSICS | CHANNEL | DISEASE | SECONDARY STRUCTURE | BINDING-SITES | STRUCTURE PREDICTION | AGGREGATION | Protein Structure, Tertiary | Serum Amyloid A Protein - metabolism | Peptides - chemistry | Humans | Alanine - chemistry | Cystatin C - chemistry | Proline - chemistry | Chromatography, Affinity | Peptides - metabolism | Protein Isoforms - metabolism | Serum Amyloid A Protein - chemistry | Protein Isoforms - chemistry | Cystatin C - metabolism | Calorimetry, Differential Scanning | Protein Conformation | Circular Dichroism
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